8aev - Revision history

OCA at 08:11, 7 February 2024

2024-02-07T08:11:24Z

← Older revision		Revision as of 08:11, 7 February 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8aev]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AEV FirstGlance]. <br>		<table><tr><td colspan='2'>[[8aev]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AEV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=LWU:1-(2-(2-((6-(dihydroxymethyl)-2-phenylpyrimidin-4-yl)methylene)hydrazineyl)-2-oxoethyl)pyridin-1-ium'>LWU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TIS:O-(1,1-DIHYDROXYETHYL)-L-SERINE'>TIS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.89Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=LWU:1-(2-(2-((6-(dihydroxymethyl)-2-phenylpyrimidin-4-yl)methylene)hydrazineyl)-2-oxoethyl)pyridin-1-ium'>LWU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TIS:O-(1,1-DIHYDROXYETHYL)-L-SERINE'>TIS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8aev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aev OCA], [https://pdbe.org/8aev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aev RCSB], [https://www.ebi.ac.uk/pdbsum/8aev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aev ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8aev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aev OCA], [https://pdbe.org/8aev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aev RCSB], [https://www.ebi.ac.uk/pdbsum/8aev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aev ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref>		[https://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	We report the implementation of coordination complexes containing two types of cationic moieties, i. e. pyridinium and ammonium quaternary salt, as potential inhibitors of human cholinesterase enzymes. Utilization of ligands containing NNO-coordination site and binding zinc metal ion allowed mono- and tetra-nuclear complexes to be obtained with corner and grid structural type, respectively, thus affecting the overall charge of the compounds (from +1 to +8). We were able to examine for the first time the multivalency effect of metallosupramolecular species on their inhibitory abilities towards acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Importantly, resolution of the crystal structures of the obtained enzyme-substrate complexes provided a better understanding of the inhibition process at the molecular level.

	Grid-Type Quaternary Metallosupramolecular Compounds Inhibit Human Cholinesterases through Dynamic Multivalent Interactions.,Nachon F, Brazzolotto X, Dias J, Courageux C, Drozdz W, Cao XY, Stefankiewicz AR, Lehn JM Chembiochem. 2022 Dec 5;23(23):e202200456. doi: 10.1002/cbic.202200456. Epub 2022 , Nov 2. PMID:36193860<ref>PMID:36193860</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 8aev" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:15, 14 June 2023

2023-06-14T08:15:01Z

← Older revision		Revision as of 08:15, 14 June 2023
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	~~'''Unreleased structure'''~~

	~~The entry~~ 8aev is ~~ON HOLD until Paper~~ Publication		==Human acetylcholinesterase in complex with N,N,N-trimethyl-2-oxo-2-(2-(pyridin-2-ylmethylene)hydrazineyl)ethan-1-aminium==
			<StructureSection load='8aev' size='340' side='right'caption='[[8aev]], [[Resolution\|resolution]] 2.89Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[8aev]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AEV FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=LWU:1-(2-(2-((6-(dihydroxymethyl)-2-phenylpyrimidin-4-yl)methylene)hydrazineyl)-2-oxoethyl)pyridin-1-ium'>LWU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TIS:O-(1,1-DIHYDROXYETHYL)-L-SERINE'>TIS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
			<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8aev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aev OCA], [https://pdbe.org/8aev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aev RCSB], [https://www.ebi.ac.uk/pdbsum/8aev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aev ProSAT]</span></td></tr>
			</table>
			== Function ==
			[https://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			We report the implementation of coordination complexes containing two types of cationic moieties, i. e. pyridinium and ammonium quaternary salt, as potential inhibitors of human cholinesterase enzymes. Utilization of ligands containing NNO-coordination site and binding zinc metal ion allowed mono- and tetra-nuclear complexes to be obtained with corner and grid structural type, respectively, thus affecting the overall charge of the compounds (from +1 to +8). We were able to examine for the first time the multivalency effect of metallosupramolecular species on their inhibitory abilities towards acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Importantly, resolution of the crystal structures of the obtained enzyme-substrate complexes provided a better understanding of the inhibition process at the molecular level.

	~~Authors:~~ Nachon, F., Dias, J., ~~Brazzolotto, X~~.		Grid-Type Quaternary Metallosupramolecular Compounds Inhibit Human Cholinesterases through Dynamic Multivalent Interactions.,Nachon F, Brazzolotto X, Dias J, Courageux C, Drozdz W, Cao XY, Stefankiewicz AR, Lehn JM Chembiochem. 2022 Dec 5;23(23):e202200456. doi: 10.1002/cbic.202200456. Epub 2022 , Nov 2. PMID:36193860<ref>PMID:36193860</ref>

	~~Description: Human acetylcholinesterase in complex with N~~,~~N,N~~-~~trimethyl~~-~~2-oxo-2-(2-(pyridin-2-ylmethylene)hydrazineyl)ethan-1-aminium~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	[[Category: ~~Unreleased Structures~~]]		</div>
	[[Category: ~~Nachon, F~~]]		<div class="pdbe-citations 8aev" style="background-color:#fffaf0;"></div>
	[[Category: Brazzolotto, X]]		== References ==
	[[Category: Dias, J]]		<references/>
			__TOC__
			</StructureSection>
			[[Category: Homo sapiens]]
			[[Category: Large Structures]]
			[[Category: Brazzolotto X]]
			[[Category: Dias J]]
			[[Category: Nachon F]]

OCA at 03:43, 18 August 2022

2022-08-18T03:43:47Z

← Older revision		Revision as of 03:43, 18 August 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8aev is ON HOLD		The entry 8aev is ON HOLD until Paper Publication

	Authors: Nachon, F., Dias, J., Brazzolotto, X.		Authors: Nachon, F., Dias, J., Brazzolotto, X.

OCA: Protected "8aev" [edit=sysop:move=sysop]

2022-07-20T04:20:14Z

Protected "8aev" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:20, 20 July 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8aev is ON HOLD Authors: Nachon, F., Dias, J., Brazzolotto, X. Description: Human acetylcholinesterase in complex with N,N,N-trimethyl-2-oxo-2-(2-(...

2022-07-20T04:20:12Z

New page: '''Unreleased structure''' The entry 8aev is ON HOLD Authors: Nachon, F., Dias, J., Brazzolotto, X. Description: Human acetylcholinesterase in complex with N,N,N-trimethyl-2-oxo-2-(2-(...

New page

'''Unreleased structure'''

The entry 8aev is ON HOLD

Authors: Nachon, F., Dias, J., Brazzolotto, X.

Description: Human acetylcholinesterase in complex with N,N,N-trimethyl-2-oxo-2-(2-(pyridin-2-ylmethylene)hydrazineyl)ethan-1-aminium
[[Category: Unreleased Structures]]
[[Category: Nachon, F]]
[[Category: Brazzolotto, X]]
[[Category: Dias, J]]